CHMP1B

CHMP1B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3EAB, 4TXQ, 4TXR, 3JC1
Identifiers
Aliases	CHMP1B , C10orf2, C18-ORF2, C18orf2, CHMP1.5, Vps46-2, Vps46B, hVps46-2, charged multivesicular body protein 1B
External IDs	OMIM: 606486 MGI: 1914314 HomoloGene: 41374 GeneCards: CHMP1B
Gene location (Human)
Chr.	Chromosome 18 (human)
End	11,854,444 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	67,340,960 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; tibialis anterior muscle; ; popliteal artery; ; biceps brachii; ; monocyte; ; right ventricle; ; gallbladder; ; stromal cell of endometrium; ; deltoid muscle; ; rectum;
	Top expressed in
	left colon; ; conjunctival fornix; ; medial ganglionic eminence; ; blood; ; thymus; ; duodenum; ; jejunum; ; intestinal villus; ; epithelium of stomach; ; seminal vesicula;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein domain specific binding ; protein binding ; identical protein binding ;
Cellular component	cytoplasm ; ESCRT III complex ; cytosol ; endosome ; late endosome membrane ; membrane ; membrane coat ; endosome membrane ; extracellular exosome ; nucleus ; midbody ; multivesicular body ;
Biological process	regulation of centrosome duplication ; nucleus organization ; establishment of protein localization ; multivesicular body assembly ; regulation of mitotic spindle assembly ; cell division ; protein transport ; cell cycle ; septum digestion after cytokinesis ; mitotic metaphase plate congression ; vacuolar transport ; ESCRT III complex disassembly ; transport ; viral budding via host ESCRT complex ; endosome transport via multivesicular body sorting pathway ; late endosome to vacuole transport ; midbody abscission ;
	Sources:Amigo / QuickGO
Orthologs
	57132
	67064
	ENSG00000255112
	ENSMUSG00000109901
	Q7LBR1
	Q99LU0
	NM_020412
	NM_024190
	NP_065145
	NP_077152
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated February 17, 2024

Charged multivesicular body protein 1b is a protein that in humans is encoded by the CHMP1B gene.^[5]^[6]

Related Research Articles

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Charged multivesicular body protein 2b is a protein that in humans is encoded by the CHMP2B gene. It forms part of one of the endosomal sorting complexes required for transport (ESCRT) - specifically ESCRT-III - which are a series of complexes involved in cell membrane remodelling. CHMP2B forms long chains that spiral around the neck of a budding vesicle. Along with the other components of ESCRT-III, CHMP2B constricts the neck of the vesicle just before it is cleaved away from the membrane.

Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.

Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.

Vacuolar protein sorting-associated protein 4B is a protein that in humans is encoded by the VPS4B gene.

Cyclin dependent kinase 13 is an enzyme that in humans is encoded by the CDK13 gene.

Vacuolar protein sorting-associated protein 28 homolog is a protein that in humans is encoded by the VPS28 gene.

Charged multivesicular body protein 4b is a protein that in humans is encoded by the CHMP4B gene.

Charged multivesicular body protein 4a is a protein that in humans is encoded by the CHMP4A gene.

Charged multivesicular body protein 5 is a protein that in humans is encoded by the CHMP5 gene.

Charged multivesicular body protein 6 is a protein that in humans is encoded by the CHMP6 gene.

Charged multivesicular body protein 2a is a protein that in humans is encoded by the CHMP2A gene.

It is a reference gene.

Charged multivesicular body protein 1a is a protein that in humans is encoded by the CHMP1A gene.

Vacuolar protein-sorting-associated protein 36 is a protein that in humans is encoded by the VPS36 gene.

Beta-catenin-like protein 1 is a protein that in humans is encoded by the CTNNBL1 gene.

Vacuolar-sorting protein SNF8 is a protein that in humans is encoded by the SNF8 gene.

Charged multivesicular body protein 4c is a protein that in humans is encoded by the CHMP4C gene.

Vacuolar protein-sorting-associated protein 25 is a protein that in humans is encoded by the VPS25 gene.

The endosomal sorting complexes required for transport (ESCRT) machinery is made up of cytosolic protein complexes, known as ESCRT-0, ESCRT-I, ESCRT-II, and ESCRT-III. Together with a number of accessory proteins, these ESCRT complexes enable a unique mode of membrane remodeling that results in membranes bending/budding away from the cytoplasm. These ESCRT components have been isolated and studied in a number of organisms including yeast and humans. A eukaryotic signature protein, the machinery is found in all eukaryotes and some archaea.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000255112 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000109901 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (Dec 2004). "The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B". Hum Mol Genet. 14 (1): 19–38. doi:10.1093/hmg/ddi003. PMID 15537668.
↑ "Entrez Gene: CHMP1B chromatin modifying protein 1B".

External links

Human C10orf2 genome location and C10orf2 gene details page in the UCSC Genome Browser .
Human CHMP1B genome location and CHMP1B gene details page in the UCSC Genome Browser .
Overview of all the structural information available in the PDB for UniProt : Q7LBR1 (Charged multivesicular body protein 1b) at the PDBe-KB .

Vuoristo JT, Berrettini WH, Ala-Kokko L (2001). "C18orf2, a novel, highly conserved intronless gene within intron 5 of the GNAL gene on chromosome 18p11". Cytogenet. Cell Genet. 93 (1–2): 19–22. doi:10.1159/000056940. PMID 11474171. S2CID 42139322.
Stauffer DR, Howard TL, Nyun T, Hollenberg SM (2002). "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression". J. Cell Sci. 114 (Pt 13): 2383–93. doi:10.1242/jcs.114.13.2383. PMID 11559747.
Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Strack B, Calistri A, Craig S, et al. (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi: 10.1016/S0092-8674(03)00653-6 . PMID 14505569. S2CID 10733770.
von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi: 10.1016/S0092-8674(03)00714-1 . PMID 14505570. S2CID 16894972.
Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. Bibcode:2003PNAS..10012414M. doi: 10.1073/pnas.2133846100 . PMC 218772 . PMID 14519844.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Scott A, Gaspar J, Stuchell-Brereton MD, et al. (2005). "Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A". Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13813–8. Bibcode:2005PNAS..10213813S. doi: 10.1073/pnas.0502165102 . PMC 1236530 . PMID 16174732.
Tsang HT, Connell JW, Brown SE, et al. (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
Row PE, Liu H, Hayes S, et al. (2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation" (PDF). J. Biol. Chem. 282 (42): 30929–37. doi: 10.1074/jbc.M704009200 . PMID 17711858.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000255112 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000109901 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid15537668-5] Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (Dec 2004). "The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B". Hum Mol Genet. 14 (1): 19–38. doi:10.1093/hmg/ddi003. PMID 15537668.

[entrez-6] "Entrez Gene: CHMP1B chromatin modifying protein 1B".

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CHMP1B

Contents

Related Research Articles

References

External links

Further reading